› 5ko0

Electron crystallography
1.4Å resolution

Human Islet Amyloid Polypeptide Segment 15-FLVHSSNNFGA-25 Determined by MicroED

Released:
DOI: 10.2210/pdb5ko0/pdb
PDB entry 5ko0 coloured by chain, front view.
PDB entry 5ko0 coloured by chain, side view.
PDB entry 5ko0 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Atomic structures of fibrillar segments of hIAPP suggest tightly mated β-sheets are important for cytotoxicity.
Krotee P, Rodriguez JA, Sawaya MR, Cascio D, Reyes FE, Shi D, Hattne J, Nannenga BL, Oskarsson ME, Philipp S, Griner S, Jiang L, Glabe CG, Westermark GT, Gonen T, Eisenberg DS
Elife 6 (2017)
PMID: 28045370
Related structures: EMD-8273

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo octadecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145619 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Islet amyloid polypeptide Chains: A, B
Molecule details ›
Chains: A, B
Length: 11 amino acids
Theoretical weight: 1.19 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P10997 (Residues: 48-58; Coverage: 16%)
Gene name: IAPP

Ligands and Environments

1 bound ligand:
Ligand SCN 1 x SCN
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 1.4Å
Relevant EMDB volumes: EMD-8273
Expression system: Not provided

Quick links

Citations

18 review citations

A new era for understanding amyloid structures and disease.
Iadanza et al. (2018)
17 more

4 mentions without citation

Electron Diffraction of 3D Molecular Crystals.
Saha et al. (2022)
3 more